Protein function and flexibility is directly related to the native distribution of its structural
elements and any alteration in protein architecture leads to several abnormalities and …

Amyloids are a class of insoluble proteinaceous substances generally composed of linear
un-branched fibrils that are formed from misfolded proteins. Conformational diseases such …

Protein crucial function and flexibility directly depend on its whole structure which is
determined by the native distribution of structural elements. Any disturbances in a protein …

Several human neurodegenerative diseases such as Alzheimer's disease, Parkinson's
disease and Familial Amyloidotic Polyneuropathy, have long been associated with …

Understanding the mechanisms underlying protein misfolding and aggregation has become
a central issue in biology and medicine. Compelling evidence show that the formation of …

Amyloidogenic diseases are characterised by the formation of amyloid aggregates inside or
outside the cell. Amyloid-associated human diseases include Alzheimer's disease …

The progression of many neurodegenerative diseases is assumed to be caused by
misfolding of specific characteristic diseases related proteins, resulting in aggregation and …

The aggregation of specific proteins is hypothesized to cause several pathological
conditions, which are collectively known as amyloid disorders. The aggregation of peptides …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

The misfolding of normally soluble proteins causes their aggregation and deposition in the
tissues which disrupts the normal structure and function of the corresponding organs. The …